Evidence map›Paper›PMID 15367757›Full record

ReviewScience's STKE : signal transduction knowledge environment2004

Human RAS superfamily proteins and related GTPases.

John Colicelli

Abstract readReview
In one paragraph

Review in Science's STKE : signal transduction knowledge environment, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 431 papers.

0numbers the graph read from it
0cells of the map it votes in
431citing papers in PubMed
9.4field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

431 citing papers in PubMed, 828 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
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  5. Review
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  8. Review
  9. Article
  10. RRAS and RRAS2 Mutations Are Recurrent Oncogenic Drivers in Lung Cancer and Are Sensitive to the Pan-RAS Inhibitor RMC-6236.Clinical cancer research : an official journal of the American Association for Cancer Research · 2026
    Article
  11. Phosphatidylinositol 4,5-bisphosphate mediates Arl4D self-interaction to promote Pak1 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  12. Ovarian Cancer Susceptibility and Chemosensitivity to KRAS Modulation.International journal of molecular sciences · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Clinically observedbioRxiv : the preprint server for biology · 2025
    Article
  18. Review
  19. Article
  20. Article

371 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

John ColicelliDepartment of Biological Chemistry and Molecular Biology Institute, University of California Los Angeles, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095, USA. colicelli@mednet.ucla.edu <colicelli@mednet.ucla.edu>
University of California, Los Angeles · US

Funding

Mechanism of RIN1 Signaling in Neuronal PlasticityR01NS046787 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI COLICELLI, JOHN J. · 2003 to 2007
$1.4M
NINDS NIH HHS R01 NS046787
6 · The paper itself

Abstract

The tumor oncoproteins HRAS, KRAS, and NRAS are the founding members of a larger family of at least 35 related human proteins. Using a somewhat broader definition of sequence similarity reveals a more extended superfamily of more than 170 RAS-related proteins. The RAS superfamily of GTP (guanosine triphosphate) hydrolysis-coupled signal transduction relay proteins can be subclassified into RAS, RHO, RAB, and ARF families, as well as the closely related Galpha family. The members of each family can, in turn, be arranged into evolutionarily conserved branches. These groupings reflect structural, biochemical, and functional conservation. Recent findings have provided insights into the signaling characteristics of representative members of most RAS superfamily branches. The analysis presented here may serve as a guide for predicting the function of numerous uncharacterized superfamily members. Also described are guanosine triphosphatases (GTPases) distinct from members of the RAS superfamily. These related proteins employ GTP binding and GTPase domains in diverse structural contexts, expanding the scope of their function in humans.

Indexed as

Amino Acid SequenceAnimalsGTP PhosphohydrolasesHumansMolecular Sequence DataProto-Oncogene Proteins p21(ras)Sequence AlignmentGTP PhosphohydrolasesHRAS protein, humanProto-Oncogene Proteins p21(ras)

Identifiers

PMID15367757
PMCPMC2828947
OpenAlexW2094585531

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.